SitesBLAST
Comparing WP_029907839.1 NCBI__GCF_000711315.1:WP_029907839.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
Q96255 Phosphoserine aminotransferase 1, chloroplastic; AtPSAT1; Phosphohydroxythreonine aminotransferase; EC 2.6.1.52 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
45% identity, 98% coverage: 7:366/367 of query aligns to 74:429/430 of Q96255
- AT 145:146 (= AT 78:79) binding
- W171 (= W105) binding
- T221 (= T155) binding
- D241 (= D175) binding
- Q264 (= Q198) binding
- K265 (= K199) modified: N6-(pyridoxal phosphate)lysine
- NT 306:307 (= NT 242:243) binding
6czyA Crystal structure of arabidopsis thaliana phosphoserine aminotransferase isoform 1 (atpsat1) in complex with pyridoxamine-5'- phosphate (pmp) (see paper)
45% identity, 99% coverage: 3:366/367 of query aligns to 2:361/362 of 6czyA
6czzA Crystal structure of arabidopsis thaliana phosphoserine aminotransferase isoform 1 (atpsat1) in complex with plp- phosphoserine geminal diamine intermediate (see paper)
45% identity, 98% coverage: 7:366/367 of query aligns to 4:359/360 of 6czzA
- binding pyridoxal-5'-phosphate: G74 (= G77), A75 (= A78), T76 (= T79), W101 (= W105), T151 (= T155), D171 (= D175), S173 (= S177), Q194 (= Q198), K195 (= K199), N236 (= N242), T237 (= T243)
- binding phosphoserine: W101 (= W105), T151 (= T155), K195 (= K199), H326 (= H333), R327 (= R334), R333 (= R340)
4azjA Structural basis of l-phosphoserine binding to bacillus alcalophilus phosphoserine aminotransferase (see paper)
45% identity, 97% coverage: 7:363/367 of query aligns to 5:357/360 of 4azjA
- active site: W102 (= W105), D172 (= D175), K196 (= K199)
- binding pyridoxal-5'-phosphate: A76 (= A78), S77 (≠ T79), W102 (= W105), T152 (= T155), D172 (= D175), S174 (= S177), Q195 (= Q198), K196 (= K199), N237 (= N242), T238 (= T243)
- binding phosphoserine: H41 (= H43), R42 (= R44), W102 (= W105), T152 (= T155), K196 (= K199), H327 (= H333), R328 (= R334), R334 (= R340)
1bt4A Phosphoserine aminotransferase from bacillus circulans subsp. Alkalophilus
46% identity, 97% coverage: 8:364/367 of query aligns to 6:358/361 of 1bt4A
1w23B Crystal structure of phosphoserine aminotransferase from bacillus alcalophilus (see paper)
45% identity, 97% coverage: 7:363/367 of query aligns to 5:354/357 of 1w23B
- active site: W102 (= W105), D172 (= D175), K196 (= K199)
- binding magnesium ion: Y127 (= Y130), Y154 (≠ E157), H285 (≠ W294), A286 (≠ S295)
- binding pyridoxal-5'-phosphate: A76 (= A78), S77 (≠ T79), W102 (= W105), T152 (= T155), D172 (= D175), S174 (= S177), Q195 (= Q198), K196 (= K199), N234 (= N242), T235 (= T243)
8a5wC Crystal structure of the human phosphoserine aminotransferase (psat) in complex with o-phosphoserine (see paper)
42% identity, 98% coverage: 7:367/367 of query aligns to 3:364/365 of 8a5wC
8a5wA Crystal structure of the human phosphoserine aminotransferase (psat) in complex with o-phosphoserine (see paper)
42% identity, 98% coverage: 7:367/367 of query aligns to 3:364/365 of 8a5wA
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G73 (= G77), G74 (≠ A78), C75 (≠ T79), W102 (= W105), T151 (= T155), D171 (= D175), S173 (= S177), Q194 (= Q198), K195 (= K199)
- binding phosphoserine: H39 (= H43), R40 (= R44), H330 (= H333), R337 (= R340)
8a5vA Crystal structure of the human phosposerine aminotransferase (psat) (see paper)
42% identity, 98% coverage: 7:367/367 of query aligns to 3:364/365 of 8a5vA
8a5vE Crystal structure of the human phosposerine aminotransferase (psat) (see paper)
42% identity, 98% coverage: 7:367/367 of query aligns to 4:365/366 of 8a5vE
Q9Y617 Phosphoserine aminotransferase; Phosphohydroxythreonine aminotransferase; PSAT; EC 2.6.1.52 from Homo sapiens (Human) (see 6 papers)
42% identity, 98% coverage: 7:367/367 of query aligns to 8:369/370 of Q9Y617
- S43 (= S42) to R: in PSATD; reduced O-phospho-L-serine:2-oxoglutarate aminotransferase catalytic efficiency; 3-fold increase of KM for 3-phosphohydroxypyruvate; 5-fold increase of KM for L-glutamate; decreased function in L-serine biosynthesis shown through in vitro reconstruction of the phosphorylated pathway; does not affect secondary structure; does not affect dimerization; does not affect thermal stability
- H44 (= H43) binding in other chain
- R45 (= R44) binding in other chain
- Y70 (≠ F69) to N: in NLS2; uncertain significance
- G79 (≠ A78) binding ; to W: in NLS2; loss of O-phospho-L-serine:2-oxoglutarate aminotransferase activity; loss of function in L-serine biosynthesis shown through in vitro reconstruction of the phosphorylated pathway
- C80 (≠ T79) binding
- P87 (= P86) to A: has no effect on O-phospho-L-serine:2-oxoglutarate aminotransferase catalytic efficiency; does not affect KM for 3-phosphohydroxypyruvate; does not affect KM for L-glutamate; no effect on function in L-serine biosynthesis shown through in vitro reconstruction of the phosphorylated pathway; does not affect secondary structure; does not affect dimerization; does not affect thermal stability; dbSNP:rs11540974
- A99 (= A97) to V: in NLS2; does not affect secondary structure; does not affect dimerization; increased thermal stability; dbSNP:rs587777778
- D100 (≠ E98) to A: in PSATD; has no effect on O-phospho-L-serine:2-oxoglutarate aminotransferase catalytic efficiency; does not affect KM for 3-phosphohydroxypyruvate; does not affect KM for L-glutamate; does not affect secondary structure; results in increased protein aggregation as shown by dynamic light scattering; dbSNP:rs118203967
- W107 (= W105) binding
- E155 (= E154) to Q: in NLS2; uncertain significance
- T156 (= T155) binding
- D176 (= D175) binding
- S179 (= S178) to L: in NLS2; loss of O-phospho-L-serine:2-oxoglutarate aminotransferase activity; loss of function in L-serine biosynthesis shown through in vitro reconstruction of the phosphorylated pathway; dbSNP:rs587777777
- Q199 (= Q198) binding
- K200 (= K199) modified: N6-(pyridoxal phosphate)lysine
- N241 (= N242) binding in other chain
- T242 (= T243) binding in other chain
- C245 (≠ V246) to R: in NLS2; reduced O-phospho-L-serine:2-oxoglutarate aminotransferase catalytic efficiency; 9-fold increase of KM for L-glutamate; does not affect KM for 3-phosphohydroxypyruvate; decreased function in L-serine biosynthesis shown through in vitro reconstruction of the phosphorylated pathway; does not affect secondary structure; does not affect dimerization
- H335 (= H333) binding
- R336 (= R334) binding
- R342 (= R340) binding ; to W: in NLS2; loss of O-phospho-L-serine:2-oxoglutarate aminotransferase activity; loss of function in L-serine biosynthesis shown through in vitro reconstruction of the phosphorylated pathway; dbSNP:rs202103028
6xdkD Crystal structure of phosphoserine aminotransferase (serc) from stenotrophomonas maltophilia k279a
43% identity, 98% coverage: 7:366/367 of query aligns to 3:358/359 of 6xdkD
8a5wE Crystal structure of the human phosphoserine aminotransferase (psat) in complex with o-phosphoserine (see paper)
41% identity, 98% coverage: 7:367/367 of query aligns to 4:364/365 of 8a5wE
- binding (2S)-2-[(E)-[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]-3-phosphonooxy-propanoic acid: H40 (= H43), R41 (= R44), N236 (= N242), T237 (= T243)
- binding (2~{S})-2-[[(~{R})-[[(5~{S})-5-azanyl-6-oxidanylidene-hexyl]amino]-[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methyl]amino]-3-phosphonooxy-propanoic acid: G74 (= G77), G75 (≠ A78), C76 (≠ T79), W103 (= W105), T152 (= T155), S174 (= S177), A194 (= A197), Q195 (= Q198), N196 (= N200), H330 (= H333), R331 (= R334), R337 (= R340), Y341 (= Y344)
3e77A Human phosphoserine aminotransferase in complex with plp
41% identity, 96% coverage: 16:367/367 of query aligns to 10:362/363 of 3e77A
- active site: W100 (= W105), D169 (= D175), K193 (= K199)
- binding pyridoxal-5'-phosphate: G71 (= G77), G72 (≠ A78), C73 (≠ T79), W100 (= W105), T149 (= T155), D169 (= D175), S171 (= S177), Q192 (= Q198), K193 (= K199), N234 (= N242), T235 (= T243)
6xdkB Crystal structure of phosphoserine aminotransferase (serc) from stenotrophomonas maltophilia k279a
43% identity, 98% coverage: 7:366/367 of query aligns to 3:354/355 of 6xdkB
3qboB Crystal structure of phosphoserine aminotransferase from yersinia pestis co92
43% identity, 98% coverage: 8:366/367 of query aligns to 4:358/359 of 3qboB
1bjoA The structure of phosphoserine aminotransferase from e. Coli in complex with alpha-methyl-l-glutamate (see paper)
42% identity, 98% coverage: 7:366/367 of query aligns to 3:359/360 of 1bjoA
- active site: W100 (= W105), D172 (= D175), K196 (= K199)
- binding alpha-methyl-l-glutamic acid: S7 (≠ A11), W100 (= W105), T151 (= T155), K196 (= K199)
- binding pyridoxal-5'-phosphate: G74 (≠ A78), R75 (≠ T79), W100 (= W105), T151 (= T155), D172 (= D175), S174 (= S177), Q195 (= Q198), K196 (= K199)
7t7jB Crystal structure of phosphoserine aminotransferase from klebsiella pneumoniae subsp. Pneumoniae in complex with pyridoxal phosphate
42% identity, 98% coverage: 8:366/367 of query aligns to 4:359/360 of 7t7jB
- binding pyridoxal-5'-phosphate: G73 (= G77), G74 (≠ A78), R75 (≠ T79), W100 (= W105), T151 (= T155), D172 (= D175), S174 (= S177), Q195 (= Q198), K196 (= K199), N237 (= N242), T238 (= T243)
5yb0B Crystal structure of wild type phosphoserine aminotransferase (psat) from e. Histolytica (see paper)
40% identity, 97% coverage: 8:364/367 of query aligns to 3:349/349 of 5yb0B
3qm2B 2.25 angstrom crystal structure of phosphoserine aminotransferase (serc) from salmonella enterica subsp. Enterica serovar typhimurium
40% identity, 98% coverage: 7:366/367 of query aligns to 3:330/331 of 3qm2B
Query Sequence
>WP_029907839.1 NCBI__GCF_000711315.1:WP_029907839.1
MKNLNELNFSAGPGALPETVLNQVQESILTLPETGMSVLGMSHRSDWFSSVLEEAETNIR
QLLGIGEEFHVLFLQGGATQQFSMIPITLLRNTGREAEYLQTGYWGKKAIVEAEKEGKVK
TLWSGQADGYKRLPDDAELSFSEQAAYLHYASNETVEGLQFHRVLGPDSVPRVCDMSSDF
LSRPVDADRFSIIYAHAQKNIGPAGVTVVLIKKSLLDSAQEQPNLPSFLDYRNHVATHSN
YNTPPVFAIYVTLLVTRWIKDVVGGLENMENINHRKAELLYQAIDDSQGFYQGWSRKEDR
SYMNATFNLTTPELEQRFLQEAAQAGFSGLDGHRSLGGVRASLYNGLTVPAVEQLLDFMS
TFERKHR
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SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory